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Magnetic Properties of [FeFe]-Hydrogenases: A Theoretical Investigation Based on Extended QM and QM/MM Models of the H-Cluster and Its Surroundings

Greco, Claudio; Silakov, Alexey; Bruschi, Maurizio; Ryde, Ulf LU ; De Gioia, Luca and Lubitz, Wolfgang (2011) In European Journal of Inorganic Chemistry p.1043-1049
Abstract
In the present contribution, we report a theoretical investigation of the magnetic properties of the dihydrogen-evolving enzyme [FeFe]-hydrogenase, based on both DFT models of the active site (the H-cluster, a Fe6S6 assembly including a binuclear portion directly involved in substrates binding), and QM/MM models of the whole enzyme. Antiferromagnetic coupling within the H-cluster has been treated using the broken-symmetry approach, along with the use of different density functionals. Results of g value calculations turned out to vary as a function of the level of theory and of the extension of the model. The choice of the broken-symmetry coupling scheme also had a significant influence on the calculated g values, for both the active-ready... (More)
In the present contribution, we report a theoretical investigation of the magnetic properties of the dihydrogen-evolving enzyme [FeFe]-hydrogenase, based on both DFT models of the active site (the H-cluster, a Fe6S6 assembly including a binuclear portion directly involved in substrates binding), and QM/MM models of the whole enzyme. Antiferromagnetic coupling within the H-cluster has been treated using the broken-symmetry approach, along with the use of different density functionals. Results of g value calculations turned out to vary as a function of the level of theory and of the extension of the model. The choice of the broken-symmetry coupling scheme also had a significant influence on the calculated g values, for both the active-ready (H-ox) and the CO-inhibited (H-ox-CO) enzyme forms. However, hyper-fine coupling-constant calculations were found to provide more consistent results. This allowed us to show that the experimentally detected delocalization of an unpaired electron at the binuclear subcluster in Desulfovibrio desulfuricans Hox is compatible with a weak interaction between the catalytic centre and a low-weight exogenous ligand like a water molecule. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Computer chemistry, Density functional calculations, Magnetic, properties, EPR parameters calculation, Quantum mechanics, Enzymes, Hydrogenases, Hydrogen
in
European Journal of Inorganic Chemistry
issue
7
pages
1043 - 1049
publisher
John Wiley & Sons
external identifiers
  • wos:000288099000015
  • scopus:79951872903
ISSN
1099-0682
DOI
10.1002/ejic.201001058
language
English
LU publication?
yes
id
09a0d005-0e6e-4a34-a78f-1c3004f6a669 (old id 1868502)
date added to LUP
2011-04-19 12:13:00
date last changed
2017-01-01 03:05:41
@article{09a0d005-0e6e-4a34-a78f-1c3004f6a669,
  abstract     = {In the present contribution, we report a theoretical investigation of the magnetic properties of the dihydrogen-evolving enzyme [FeFe]-hydrogenase, based on both DFT models of the active site (the H-cluster, a Fe6S6 assembly including a binuclear portion directly involved in substrates binding), and QM/MM models of the whole enzyme. Antiferromagnetic coupling within the H-cluster has been treated using the broken-symmetry approach, along with the use of different density functionals. Results of g value calculations turned out to vary as a function of the level of theory and of the extension of the model. The choice of the broken-symmetry coupling scheme also had a significant influence on the calculated g values, for both the active-ready (H-ox) and the CO-inhibited (H-ox-CO) enzyme forms. However, hyper-fine coupling-constant calculations were found to provide more consistent results. This allowed us to show that the experimentally detected delocalization of an unpaired electron at the binuclear subcluster in Desulfovibrio desulfuricans Hox is compatible with a weak interaction between the catalytic centre and a low-weight exogenous ligand like a water molecule.},
  author       = {Greco, Claudio and Silakov, Alexey and Bruschi, Maurizio and Ryde, Ulf and De Gioia, Luca and Lubitz, Wolfgang},
  issn         = {1099-0682},
  keyword      = {Computer chemistry,Density functional calculations,Magnetic,properties,EPR parameters calculation,Quantum mechanics,Enzymes,Hydrogenases,Hydrogen},
  language     = {eng},
  number       = {7},
  pages        = {1043--1049},
  publisher    = {John Wiley & Sons},
  series       = {European Journal of Inorganic Chemistry},
  title        = {Magnetic Properties of [FeFe]-Hydrogenases: A Theoretical Investigation Based on Extended QM and QM/MM Models of the H-Cluster and Its Surroundings},
  url          = {http://dx.doi.org/10.1002/ejic.201001058},
  year         = {2011},
}